ArticlePLoS pathogens2012
Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
153 citing papers in PubMed, 1 synthesis or guideline pooled it, 207 citations in OpenAlex.
- SARS-CoV-2 cell entry beyond the ACE2 receptor.Molecular biology reports · 2022Pooled it
- Temporal changes in soluble angiotensin-converting enzyme 2 associated with metabolic health, body composition, and proteome dynamics during a weight loss diet intervention: a randomized trial with implications for the COVID-19 pandemic.The American journal of clinical nutrition · 2021Trial
- Aminopeptidase N is a receptor for hedgehog merbecoviruses.Nature microbiology · 2026Article
- Structure and receptor recognition of type-II feline infectious peritonitis virus spike glycoprotein.The EMBO journal · 2026Article
- Pathogen-specific immune responses might underlie divergent outcomes of coronavirus and influenza infection in the natural porcine host.Communications biology · 2026Article
- Article
- FUT8-mediated core fucosylation of receptor APN drives entry of multiple alphacoronaviruses.PLoS pathogens · 2026Article
- Quantifying and combating zoonotic viruses poised for emergence: Using multiplex receptor screening and decoy engineering technologies.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cetacean coronavirus spikes highlight S glycoprotein structural plasticity.PLoS pathogens · 2026Article
- PEPNet: a two-stage point cloud framework with hierarchical embedding and antigen-antibody interaction modeling for epitope prediction.Briefings in bioinformatics · 2026Article
- Construction of subunit vaccine by fusingFrontiers in veterinary science · 2026Article
- First report on detection and molecular characterization of alphacoronaviruses in the small Indian mongoose (Urva auropunctata).Virology journal · 2025Article
- Review
- Article
- New Coronavirus in Colombian Caribbean Bats: In Silico Analysis Reveals Possible Risk of Interspecific Jumping.Viruses · 2025Article
- How Does Porcine Epidemic Diarrhea Virus Escape Host Innate Immunity?Pathogens (Basel, Switzerland) · 2025Review
- Metagenomic analysis of viral diversity in Portuguese bats.Veterinary research communications · 2025Article
- A novel linear B-cell epitope on S2 protein of transmissible gastroenteritis virus identified using a monoclonal antibody.BMC veterinary research · 2025Article
- Article
- Enteric viromes of healthy farmed mink (Neovison vison) from Shandong and Liaoning provinces, China.Animal microbiome · 2025Article
93 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The coronaviruses (CoVs) are enveloped viruses of animals and humans associated mostly with enteric and respiratory diseases, such as the severe acute respiratory syndrome and 10-20% of all common colds. A subset of CoVs uses the cell surface aminopeptidase N (APN), a membrane-bound metalloprotease, as a cell entry receptor. In these viruses, the envelope spike glycoprotein (S) mediates the attachment of the virus particles to APN and subsequent cell entry, which can be blocked by neutralizing antibodies. Here we describe the crystal structures of the receptor-binding domains (RBDs) of two closely related CoV strains, transmissible gastroenteritis virus (TGEV) and porcine respiratory CoV (PRCV), in complex with their receptor, porcine APN (pAPN), or with a neutralizing antibody. The data provide detailed information on the architecture of the dimeric pAPN ectodomain and its interaction with the CoV S. We show that a protruding receptor-binding edge in the S determines virus-binding specificity for recessed glycan-containing surfaces in the membrane-distal region of the pAPN ectodomain. Comparison of the RBDs of TGEV and PRCV to those of other related CoVs, suggests that the conformation of the S receptor-binding region determines cell entry receptor specificity. Moreover, the receptor-binding edge is a major antigenic determinant in the TGEV envelope S that is targeted by neutralizing antibodies. Our results provide a compelling view on CoV cell entry and immune neutralization, and may aid the design of antivirals or CoV vaccines. APN is also considered a target for cancer therapy and its structure, reported here, could facilitate the development of anti-cancer drugs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.